scholarly journals Silicone Oil- and Agitation-Induced Aggregation of a Monoclonal Antibody in Aqueous Solution

2009 ◽  
Vol 98 (9) ◽  
pp. 3167-3181 ◽  
Author(s):  
Renuka Thirumangalathu ◽  
Sampathkumar Krishnan ◽  
Margaret Speed Ricci ◽  
David N. Brems ◽  
Theodore W. Randolph ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Monoclonal Antibody ◽  
Silicone Oil ◽  
Induced Aggregation

scholarly journals Thermoresponsive Polymers as Macromolecular Coordination Ligands: Complexation-Dependence of Thermally Induced Aggregation in Aqueous Solution

2021 ◽  
Author(s):  
Maximilian Felix Toni Meier ◽  
Franck Thetiot ◽  
Narsimhulu Pittala ◽  
Ingo Lieberwirth ◽  
Cleiton Kunzler ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Thermoresponsive Polymers ◽  
Thermally Induced ◽  
Coordination Sites ◽  
Induced Aggregation

We have designed novel macromolecular coordination ligands (MCLs) by conjugation of thermoresponsive polymers based on poly(N-isopropylacrylamide) (M ̅_n around 3 to 25 kg∙mol-1) with 1,2,4-triazole coordination sites. These triazole units...

A Small-Angle X-Ray Scattering Study on Pre-Irradiated Malate Synthase. The Influence of Formate, Superoxide Dismutase, and Catalase on the X-Ray Induced Aggregation of the Enzyme

1985 ◽  
Vol 40 (5-6) ◽  
pp. 364-372 ◽  
Author(s):  
P. Zipper ◽  
R. Wilfing ◽  
M. Kriechbaum ◽  
H. Durchschlag
Keyword(s):  
Aqueous Solution ◽  
Superoxide Dismutase ◽  
Small Angle ◽  
Malate Synthase ◽  
X Ray ◽  
X Ray Scattering ◽  
X Irradiation ◽  
The Mean ◽  
Induced Aggregation ◽  
Ray Scattering

Abstract The sulfhydryl enzyme malate synthase from baker’s yeast was X-irradiated with 6 kGy in air-saturated aqueous solution (enzyme concentration: ≃ 10 mg/ml; volume: 120 μl), in the absence or presence of the specific scavengers formate, superoxide dismutase, and catalase. After X-irradiation, a small aliquot of the irradiated solutions was tested for enzymic activity while the main portion was investigated by means of small-angle X-ray scattering. Additionally, an unir­radiated sample without additives was investigated as a reference. Experiments yielded the fol­lowing results: 1. X-irradiation in the absence of the mentioned scavengers caused considerable aggregation, fragmentation, and inactivation of the enzyme. The dose Dt37 for total (= repairable + non­-repayable) inactivation resulted as 4.4 kGy. The mean radius of gyration was found to be about 13 nm. The mean degree of aggregation was obtained as 5.7, without correction for fragmenta­tion. An estimation based on the thickness factor revealed that about 19% of material might be strongly fragmented. When this amount of fragments was accordingly taken into account, a value of 7.1 was obtained as an upper limit for the mean degree of aggregation. The observed retention of the thickness factor and the finding of two different cross-section factors are in full accord with the two-dimensional aggregation model established previously (Zipper and Durchschlag, Radiat. Environ. Biophys. 18, 99 - 121 (1980)). 2. The presence of catalytic amounts of superoxide dismutase and/or catalase, in the absence of formate, during X-irradiation reduced both aggregation and inactivation significantly. 3. The presence of formate (10 or 100 mᴍ) during X-irradiation led to a strong decrease of aggregation and inactivation. This effect was more pronounced with the higher formate concen­tration or when superoxide dismutase and/or catalase were simultaneously present during X-irradiation. The presence of formate also reduced the amount of fragments significantly. 4. The results clearly show that the aggregation and inactivation of malate synthase upon X-irradiation in aqueous solution are mainly caused by OH·; to a minor extent O·̄2 and H2O2 are additionally involved in the damaging processes.

Target induced aggregation of modified Au@Ag nanoparticles for surface enhanced Raman scattering and its ultrasensitive detection of arsenic(iii) in aqueous solution

RSC Advances ◽  
2015 ◽  
Vol 5 (95) ◽  
pp. 77755-77759 ◽  
Author(s):  
Bo Yang ◽  
Xiaochun Chen ◽  
Renyong Liu ◽  
Bianhua Liu ◽  
Changlong Jiang
Keyword(s):  
Aqueous Solution ◽  
Spectroscopic Technique ◽  
Ultrasensitive Detection ◽  
Selective Detection ◽  
Raman Spectroscopic ◽  
Highly Sensitive ◽  
Surface Enhanced ◽  
Surface Enhanced Raman ◽  
Enhanced Raman Scattering ◽  
Induced Aggregation

A highly sensitive and selective detection of As(iii) was reported by target induced aggregation of nanoparticles enhanced Raman spectroscopic technique.

Gelation of a Monoclonal Antibody at the Silicone Oil–Water Interface and Subsequent Rupture of the Interfacial Gel Results in Aggregation and Particle Formation

2015 ◽  
Vol 104 (4) ◽  
pp. 1282-1290 ◽  
Author(s):  
Shyam B. Mehta ◽  
Rachael Lewus ◽  
Jared S. Bee ◽  
Theodore W. Randolph ◽  
John F. Carpenter
Keyword(s):  
Monoclonal Antibody ◽  
Silicone Oil ◽  
Particle Formation ◽  
Water Interface ◽  
Oil Water

scholarly journals Platelet membrane alterations induced by the local anesthetic dibucaine

Blood ◽  
1986 ◽  
Vol 68 (2) ◽  
pp. 463-471 ◽  
Author(s):  
EI Peerschke
Keyword(s):  
Monoclonal Antibody ◽  
Binding Sites ◽  
Periodic Acid ◽  
Platelet Membrane ◽  
Actin Binding ◽  
Scatchard Analysis ◽  
Affinity Binding ◽  
High Affinity ◽  
Fibrinogen Binding ◽  
Induced Aggregation

Abstract Tertiary amine local anesthetics modify a variety of platelet membrane- related functions. The present study explored dibucaine (DB)-induced inhibition of platelet cohesion by examining structural and functional alterations of the human platelet membrane glycoprotein IIb-IIIa complex (GPIIb-IIIa) and platelet Ca2+ homeostasis. Complete inhibition of ADP-induced aggregation was achieved five minutes after platelet exposure to 0.10 to 0.25 mmol/L of DB when fibrinogen binding was reduced by 50%. At higher concentrations of DB (approximately 1 mmol/L), ADP-induced fibrinogen binding was completely blocked. Scatchard analysis revealed loss of high-affinity binding sites in addition to reduction in Bmax. In contrast, chymotrypsin-treated platelets sustained 50% inhibition of fibrinogen binding when incubated with 0.4 to 0.5 mmol/L DB, and kinetic analysis showed that the high- affinity platelet-fibrinogen interactions were reduced but not absent. Fibrinogen binding to chymotrypsin-treated platelets could not be completely inhibited even at high DB concentrations (1 mmol/L). The inhibition of fibrinogen binding to chymotrypsin-treated platelets correlated with changes in binding of a monoclonal antibody (10E5) specific for an epitope on the GPIIb-IIIa complex. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and radioelectroimmunoassay of DB-treated platelets, however, showed no evidence of a reduction or degradation of GP IIb or IIIa. Platelet incubation with DB (five minutes, 0.1 to 1.0 mmol/L) was also accompanied by: increased platelet membrane-associated Ca2+ involving low-affinity binding sites [Kd = 5 X 10(-5) mol/L-]; increased 45Ca2+ uptake which correlated with degradation of actin-binding protein (ABP) and digestion of GPIb as visualized on periodic-acid Schiff (PAS)- stained SDS gels and as inferred from decreased binding of a monoclonal antibody (6D1) directed against this glycoprotein; and enhanced Ca2+ exchange. Thus, exposure of platelets to DB results in membrane-related alterations that may contribute to inhibition of platelet cohesion: Decreased fibrinogen receptor exposure by traditional agonists and diminished accessibility of the GPIIb-IIIa complex to extracellular ligands correlate with DB-induced inhibition of platelet aggregation; and increased calcium uptake and exchange across the platelet membrane likely leads to activation of the calcium-dependent protease(s) which was previously shown to correlate with DB-induced inhibition of ristocetin-induced platelet agglutination.

Oil-Induced Aggregation of Block Copolymer in Aqueous Solution

2007 ◽  
Vol 111 (38) ◽  
pp. 11140-11148 ◽  
Author(s):  
Jun-he Ma ◽  
Yun Wang ◽  
Chen Guo ◽  
Hui-zhou Liu ◽  
Ya-lin Tang ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Block Copolymer ◽  
Induced Aggregation

scholarly journals Temperature Induced Aggregation and Clouding in Humic Acid Solutions

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Leah Shaffer ◽  
Ray von Wandruszka
Keyword(s):  
Aqueous Solution ◽  
Light Scattering ◽  
Humic Acid ◽  
Dynamic Light Scattering ◽  
Acid Solutions ◽  
Inverse Temperature ◽  
Mechanical Agitation ◽  
Coulombic Repulsion ◽  
Polarity Sensitive ◽  
Induced Aggregation

Humic acids in aqueous solution demonstrate inverse temperature-solubility relationships when solution conditions are manipulated to reduce coulombic repulsion among the humic polyanions. These effects were followed by dynamic light scattering (DLS) measurements of the resulting aggregates, as well as the addition of a polarity sensitive fluorescent probe (pyrene). The humic solutions could be primed for temperature induced clouding by carefully lowering the pH to a point where hydration effects became dominant. The exact value of the cloud point (CP) was a function of both pH and humate concentration. The CPs mostly lay in the range 50–90°C, but DLS showed that temperature induced aggregation proceeded from approximately 30°C onward. Similar effects could be achieved by adding multivalent cations at concentrations below those which cause spontaneous precipitation. The declouding of clouded humate solutions could be affected by lowering the temperature combined with mechanical agitation to disentangle the humic polymers.

AN EPITOPE OF A MONOCLONAL ANTIBODY (TM83) AGAINST GLYCOPROTEIN lib/Ilia COMPLEX

1987 ◽  
Author(s):  
N Yamamoto ◽  
H Kitagawa ◽  
K Tanoue ◽  
H YAmazaki
Keyword(s):  
Monoclonal Antibody ◽  
Calcium Concentration ◽  
Binding Capacity ◽  
Membrane Preparation ◽  
Crossed Immunoelectrophoresis ◽  
Fibrinogen Binding ◽  
Atp Secretion ◽  
Sds Page ◽  
Triton X ◽  
Induced Aggregation

GPIIb/lIIa is forming a heterodimer complex on the human platelet membrane.Many monoclonal antibodiesagainst GPIIb/IIIa complex obtained elsewhere react with neither GPIIb nor GPIIIa separately when GPIIb/IIIa is blotted to filter after SDS-PAGE. Therefore the epitope of GPIIb/IIIa complex is not identified actually. Our attemption is to clarify the epitope recognized by a monoclonal antibody against GPIIb/IIIa designated TM83. TM83 (30 yg/ml) inhibited collagen-, ADP-, or thrombin-induced aggregation, but it did not inhibit ATP-secretion induced by 0.01 U/ml of thrombin. TM83 also inhibited fibrinogen-binding approximately to 50 % of total binding. The binding of 125 I- TM83 to platelets decreased to b0% of controlwhen platelets were incubated in the presence of 1 mM EDTA at 37°C for 30 min. However the incubation at25°C for 30 min did not change any binding capacity of 125 I-TM83 to platelets. Thus thebinding of TM83to platelets was dependent on both temperature and calcium concentration in surrouding medium, suggesting that TM83 bound to GPIIb/IIIa complex.If the small amounts of epitope of GPIIb/IIIa complex is not injured during SDS-PAGE and blotting, we may identify clearly the epitope of GPIIb/IIIa complex. For this aim, GPIIb/IIIa complex was extracted carefully in the presence of 1 mM calcium by the phase separationusing Triton X-11U, and was run on SDS-PAGE in the presence of 100 yM calcium. Western-blot of the membrane preparation showed that 125 I-TM83 was incorporated into both GPIIb and GPIIIa on Durapore filter. Further radio-crossed immunoelectrophoresis showed that I-TM83 was incorporated only into immunoprecipitin of GPIIb/IIIa complex in the presenceof 1 mM calcium. While after addition of 25 mM EDTA to the membrane preparation containing 1 mM calcium,125i-tm83 wasmainly incorporated into GPIIb/IIIa complex as well, however very faint radioactivity fromthe immunoprecipitin corresponding to GPIIIa was observed, but the radioactivity from GPIIb was not identified. While there is a discrepancy inour result, it must be further studied whether one monoclonal antibody can recognize or not two kinds of GPs, GPIIb and Ilia, which are formed in complex in physiological condition.

Effects Of A Monoclonal Antibody To Human Platelet Glycoprotein I On Platelet - Von Willebrand Factor Subendothelium Interactions

1981 ◽  
Author(s):  
C Ruan ◽  
G Tobelem ◽  
A McMichael ◽  
L Drouet ◽  
Y Legrand ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Factor Viii ◽  
Human Platelet ◽  
Rabbit Aorta ◽  
Collagen Type I ◽  
Platelet Glycoprotein ◽  
Type I ◽  
Glycoprotein I ◽  
Induced Aggregation ◽  
Willebrand Factor

A monoclonal antibody (AN51) to human platelet glycoprotein I (GPI) secreted by a hybrid myeloma has been tested on platelet functions. AN51 bound to normal and thrombasthenic platelets while it failed to bind to platelets from 6 patients with Bernard-Soulier syndrome (BSS). The nature of the antigen recognized by AN51 was determined by demonstration that the antigen, which was chymotrypsin sensitive, gave a peak at 150,000 daltons on SDS-PAGE after immunoprecipitation. AN51 strongly inhibited Ristocetin, bovine factor VIII or porcine factor VIII induced aggregation but did not modify ADP, collagen type I or type III, thrombin or arachidonic acid induced aggregations. Furthermore the adhesion-aggregation of platelet induced by microfibrils was also inhibited by the antibody AN51. Platelet adhesion to untreated or collagenase treated rabbit aorta subendothelium, using the Baumgartner technique, was impaired by AN51, and the inhibition was more pronouced at high shear rate conditions. AN51 decreased the binding of 125I-factor VIII/Willebrand factor (FVIII/WF) to human platelets in presence of Ristocetin. The use of this monoclonal antibody directed against platelet GPI permits a better understanding of the platelet-platelet and platelet-subendothelium interactions mediated by FVIII/WF and will facilitate the purification of the platelet membrane glycoprotein lacking in BSS which may be the receptor for FVIII/WF.

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